5CD8
Crystal structure of the NTD of Drosophila Oskar protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-02 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9641 |
| Spacegroup name | P 32 |
| Unit cell lengths | 66.951, 66.951, 112.831 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.434 - 3.001 |
| R-factor | 0.1918 |
| Rwork | 0.189 |
| R-free | 0.24190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5cd7 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.913 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 6.460 | 3.000 |
| Rmerge | 0.055 | 0.022 | 0.456 |
| Total number of observations | 65587 | ||
| Number of reflections | 11302 | ||
| <I/σ(I)> | 12.5 | 4.1 | |
| Completeness [%] | 99.8 | 99.1 | 99.7 |
| Redundancy | 5.8 | 5.8 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 289 | 20% PEG 400, 200mM Mg(AC)2, 100mM NaAC, pH 5.6 |






